Figure 6: Kinetic characterization of GEO 175 and GEO 175 L376T_T240S. | Nature Communications

Figure 6: Kinetic characterization of GEO 175 and GEO 175 L376T_T240S.

From: Integrative genomic mining for enzyme function to enable engineering of a non-natural biosynthetic pathway

Figure 6

Kinetic constants were measured as described in Methods. The substrate 2-ketooctanoate carbon chain numbering referred to in the text is numbered in white. According to the molecular model of GEO 175, the double mutation L376T_T240S is predicted to recede the pocket by 1.4 Å and remove interactions between the binding pocket and carbon 8 of the ketoacid alkyl chain. This mutant was observed to decrease catalytic efficiency on C8, but has a negligible effect on shorter-chain substrates. Errors are shown as ±one s.d.

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